Protein kinase and phosphoproteins of avian myeloblastosis virus

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Published inJournal of Virology Vol. 21; no. 3; pp. 843 - 848
Main Author Tsiapalis, C.M
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.03.1977
Subjects
animal diseases
animal health
Avian Leukosis Virus - enzymology
Avian Myeloblastosis Virus - enzymology
Avian Myeloblastosis Virus - metabolism
Caseins - metabolism
Molecular Weight
Peptides - metabolism
Phosphates - metabolism
Phosphoproteins - biosynthesis
Protamines - metabolism
Protein Kinases - isolation & purification
Protein Kinases - metabolism
RNA-Directed DNA Polymerase - metabolism
Viral Proteins - biosynthesis
Viral Proteins - metabolism
Online AccessGet full text
ISSN0022-538X
1098-5514
DOI10.1128/jvi.21.3.843-848.1977

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Abstract Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JVI .asm.org, visit: JVI       
AbstractList A protein kinase associated with purified virions of avian myeloblastosis virus, BAI strain A, was highly purified by ion-exchange chromatography and gel filtration. On the basis of molecular sieving on Sephadex G-200, the enzyme protein appeared to have a molecular weight of about 50,000 to 60,000; disc gel electrophoresis in sodium dodecyl sulfate-acrylamide gels revealed the presence of at least two polypeptide chains; and isoelectric focusing on acrylamide gels revealed two protein bands with activity. Of the nonviral proteins used as phosphate acceptors, the greatest rate of phosphorylation was obtained with alpha-casein. Potential physiological substrates for this activity included specific virion polypeptide of avian myeloblastosis virus. One of the virion polypeptides found in association with reverse transcriptase activity from avian myeloblastosis virus accepted more phosphate than any of nonviral or viral polypeptides examined on the basis of nanomoles of 32P incorporated per milligram of protein.
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Author Tsiapalis, C.M
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Snippet Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
A protein kinase associated with purified virions of avian myeloblastosis virus, BAI strain A, was highly purified by ion-exchange chromatography and gel...
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StartPage 843
SubjectTerms animal diseases
animal health
Avian Leukosis Virus - enzymology
Avian Myeloblastosis Virus - enzymology
Avian Myeloblastosis Virus - metabolism
Caseins - metabolism
Molecular Weight
Peptides - metabolism
Phosphates - metabolism
Phosphoproteins - biosynthesis
Protamines - metabolism
Protein Kinases - isolation & purification
Protein Kinases - metabolism
RNA-Directed DNA Polymerase - metabolism
Viral Proteins - biosynthesis
Viral Proteins - metabolism
Title Protein kinase and phosphoproteins of avian myeloblastosis virus
URI http://jvi.asm.org/content/21/3/843.abstract
https://www.ncbi.nlm.nih.gov/pubmed/66329
https://www.proquest.com/docview/2985947553
https://www.proquest.com/docview/45988183
https://pubmed.ncbi.nlm.nih.gov/PMC515621
Volume 21
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